第二种类型的卡德林ectodomain结构:对经典卡德林特异性的影响
Saurabh D Patel1, Carlo Ciatto, Chien Peter Chen
1Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Cell
|March 28, 2006
概括
经典的卡德林 (I型和II型) 中介于细胞粘附. 结构分析揭示了II型阴蛋白中独特的粘合接口,由交换的β链和保存的托残留物驱动,决定了细胞特异性.
科学领域:
- 细胞生物学 细胞生物学
- 结构生物学是结构生物学.
- 生物化学 生物化学
背景情况:
- 经典的卡德林 (I型和II型) 是关键的细胞粘附分子.
- 它们的细胞外域决定了细胞对细胞的识别和特异性.
研究的目的:
- 阐明II型古典干素细胞粘附特异性的结构基础.
- 为了比较I型和II型卡德林的粘合接口.
主要方法:
- 从三种II型阴蛋白中确定ectodomain区域的晶体结构.
- 蛋白界面和保存残留物的分析.
- 在体外和体内活体功能测定中使用了仿真.
主要成果:
- 二型卡德林通过其细胞外卡德林-1 (EC1) 域中的交换的N端β链形成粘合性二次体.
- 这些接口具有两种保存的托残留物和独特的疏水区域,与I型卡德林不同.
- 无论是I型还是II型阴蛋白的EC1域在体外都决定了细胞粘合特异性.
- 化学阴素实验表明,EC1域身份对于II型阴素在体内运动神经元分离中的功能至关重要.
结论:
- 该EC1域,特别是其结构定义的粘合接口,编码的功能特异性为II型cadherins in vivo.
- 在EC1域界面中的结构差异有助于I型和II型卡德林的独特粘合性能.
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